Crystal structure of theStreptococcus agalactiaeCAMP factor, and insights into its membrane-permeabilizing activity

Toxin from group B streptococcus decoded

25 April 2019

Researchers have elucidated the structure of the bacterial protein used to diagnose group B streptococcal infections, and this has helped clarify the mechanism by which the toxic protein perforates and destroys red blood cells.

The ‘CAMP test’ used to identify group B streptococcal infections relies on the fact that the blood-bursting ability of an unrelated bacterium is enhanced in the presence the pore-forming toxin CAMP factor from Streptococcus agalactiae, the bug responsible for group B strep.

Now, a team co-led by investigators from the University of Science and Technology of China has determined the atomic structure of the CAMP factor. This has revealed the section of the protein involved in making cell membranes permeable and the region needed for promoting the breakdown of blood cells.

The findings could lead to new diagnostic tests and treatments for group B strep.

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References

1. Journal of Biological Chemistry 293, 11867–11877 (2018). doi: 10.1074/jbc.RA118.002336